Formation of Critical Oligomers Is a Key Event during Conformational Transition of Recombinant Syrian Hamster Prion Protein

Journal of Biological Chemistry

Volumn 278, Issue 42, 2003, Pages 40481-40492

  Sokolowski, Fabian ^a,b   Modler, Andreas Johannes ^c,d   Masuch, Ralf ^e,f   Zirwer, Dietrich ^c   Baier, Michael ^a   Lutsch, Gudrun ^c   Moss, David Alan ^e   Gast, Klaus ^c   Naumann, Dieter ^a  

^a ROBERT KOCH INSTITUTE   (Germany)

^b FREIE UNIVERSITÄT BERLIN   (Germany)

^c MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^d HUMBOLDT UNIVERSITY   (Germany)

^e KARLSRUHE INSTITUTE OF TECHNOLOGY   (Germany)

^f Micro biolytics GmbH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; CONFORMATIONS; ELECTRON MICROSCOPY; FOURIER TRANSFORM INFRARED SPECTROSCOPY; HYDROGEN BONDS; LIGHT SCATTERING; MOLECULAR STRUCTURE; OLIGOMERS; PHASE TRANSITIONS; REACTION KINETICS;

CONFORMATIONAL TRANSITIONS;

PROTEINS;

AMIDE; GUANIDINE; OLIGOMER; PRION PROTEIN; RECOMBINANT SYRIAN HAMSTER PRION PROTEIN[90-232]; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; ELECTRON MICROSCOPY; EQUILIBRIUM CONSTANT; FOURIER TRANSFORMATION; HYDROGEN BOND; INFRARED SPECTROSCOPY; KINETICS; LIGHT SCATTERING; MOLECULAR MODEL; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN UNFOLDING; REACTION ANALYSIS;

ANIMALS; CIRCULAR DICHROISM; CRICETINAE; DOSE-RESPONSE RELATIONSHIP, DRUG; GUANIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; LIGHT; MESOCRICETUS; MICROSCOPY, ELECTRON; PRIONS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SCATTERING, RADIATION; SODIUM ACETATE; SODIUM CHLORIDE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TIME FACTORS;

CRICETINAE; MESOCRICETUS AURATUS;

EID: 0142040121     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M304391200     Document Type: Article

References (55)

1. Prusiner, S. B. (1982) Science 216, 136-144
2. Prusiner, S. B. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 13363-13383
3. Wisniewski, T., Aucouturier, P., Soto, C., and Frangione, B. (1998) Amyloid 5, 212-224
4. Caughey, B. W., Dong, A., Bhat, K. S., Ernst, D., Hayes, S. F., and Caughey, W. S. (1991) Biochemistry 30, 7672-7680
5. Pan, K.-M., Baldwin, M. A., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Huang, Z., Fletterick, R. J., Cohen, F. E., and Prusiner, S. B. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 10962-10966
6. Chiesa, R., and Harris, D. A. (2001) Neurobiol. Dis. 8, 743-763
7. Ma, J., Wollmann, R., and Lindquist, S. (2002) Science 298, 1781-1785
8. Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T., and Lansbury, P. T., Jr. (2002) Nature 418, 291
9. Morillas, M., Vanik, D. L., and Surewicz, W. K. (2001) Biochemistry 40, 6982-6987
10. Baskakov, I. V., Legname, G., Baldwin, M. A., Prusiner, S. B., and Cohen, F. E. (2002) J. Biol. Chem. 277, 21140-21148
11. Lu, B.-Y., and Chang, J.-Y. (2002) Biochem. J. 364, 81-87
12. Hornemann, S., Korth, C., Oesch, B., Riek, R., Wider, G., Wüthrich, K., and Glockshuber, R. (1997) FEBS Lett. 413, 277-281
13. Jackson, G. S., Hill, A. F., Joseph, C., Hosszu, L., Power, A., Waltho, J. P., Clarke, A. R., and Collinge, J. (1999) Biochim. Biophys. Acta. 1431, 1-13
14. Zahn, R., van Schroetter, C., and Wüthrich, K. (1997) FEBS Lett. 417, 400-404
15. Mehlhorn, I., Groth, D., Stöckel, J., Moffat, B., Yansura, D. R. D., Willett, W. S., Baldwin, M., Fletterick, R., Cohen, F. E., Vandlen, R., Henner, D., and Prusiner, S. B. (1996) Biochemistry 35, 5528-5537
16. Alvarez-Martinez, M. T., Torrent, J., Lange, R., Verdier, J.-M., Balny, C., and Liautard, J.-P. (2003) Biochim. Biophys. Acta. 1645, 228-240
17. Masuch, R., and Moss, D. A. (2003) Appl. Spectroscopy 57, in press
18. Savitzky, A., and Golay, M. J. E. (1964) Anal. Chem. 36, 1627-1639
19. Gast, K., Nöppert, A., Müller-Frohne, M., Zirwer, D., and Damaschun, G. (1997) Eur. Biophys. J. 25, 211-219
20. Provencher, S. W. (1982) Comput. Phys. Commun. 27, 229-242
21. Koppel, D. E. (1972) J. Chem. Phys. 57, 4814-4820
22. Johnson Jr., W. C. (1990) Proteins 7, 205-214
23. Mauser, H. (1974) Formale Kinetik, Bertelsmann Universitätsverlag, Düsseldorf, Germany
24. Krimm, S., and Bandekar, J. (1986) Adv. Protein Chem. 38, 181-364
25. Fabian, H., and Mäntele, W. (2002) in Handbook of Vibrational Spectroscopy (Chalmers, J. M., and Griffiths, P. R., eds) Vol. 5, pp. 3399-3425, John Wiley & Sons, Ltd., Chichester, UK
26. Barth, A., and Zscherp, C. (2002) Q. Rev. Biophys. 35, 369-430
27. Jackson, M., and Mantsch, H. H. (1995) Crit. Rev. Biochem. Mol. Biol. 30, 95-120
28. Barth, A. (2000) Prog. Biophys. Mol. Biol. 74, 141-173
29. Zahn, R., Liu, A., Lührs, T., Riek, R., von Schroetter, C., García, F. L., Billeter, M., Calzolai, L., Wider, G., and Wüthrich, K. (2000) Proc. Natl. Acad. Sci. U. S. A. 97, 145-150
30. Wüthrich, K., and Riek, R. (2001) Adv. Protein Chem. 57, 55-82
31. Glockshuber, R. (2001) Adv. Protein Chem. 57, 83-105
32. Swietnicki, W., Petersen, R., Gambetti, P., and Surewicz, W. K. (1997) J. Biol. Chem. 272, 27517-27520
33. Zhang, H., Stöckel, J., Mehlhorn, I., Groth, D., Baldwin, M. A., Prusiner, S. B., James, T. L., and Cohen, F. E. (1997) Biochemistry 36, 3543-3553
34. Hornemann, S., and Glockshuber, R. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 6010-6014
35. Kubelka, J., and Keiderling, T. A. (2001) J. Am. Chem. Soc. 123, 12048-12058
36. Henry, E. R., and Hofrichter, J. (1992) Methods Enzymol. 210, 129-192
37. Baskakov, I. V., Aagaard, C., Mehlhorn, I., Wille, H., Groth, D., Baldwin, M. A., Prusiner, S. B., and Cohen, F. E. (2000) Biochemistry 39, 2792-2804
38. Baskakov, I. V., Legname, G., Prusiner, S. B., and Cohen, F. E. (2001) J. Biol. Chem. 276, 19687-19690
39. Xiong, L.-W., Raymond, L. D., Hayes, S. F., Raymond, G. J., and Caughey, B. (2001) J. Neurochem. 79, 669-678
40. Callaham, M. A., Xiong, L.-W., and Caughey, B. (2001) J. Biol. Chem. 276, 28022-28028
41. Sanghera, N., and Pinheiro, T. J. T. (2002) J. Mol. Biol. 315, 1241-1256
42. Swietnicki, W., Morillas, M., Chen, S. G., Gambetti, P., and Surewicz, W. K. (2000) Biochemistry 39, 424-431
43. Yamada, N., Ariga, K., Naito, M., Matsubara, K., and Koyama, E. (1998) J. Am. Chem. Soc. 120, 12192-12199
44. Chitnumsub, P., Fiori, W. R., Lashuel, H. A., Diaz, H., and Kelly, J. W. (1999) Bioorg. Med. Chem. 7, 39-59
45. Caughey, B., Raymond, G. J., and Bessen, R. A. (1998) J. Biol. Chem. 273, 32230-32235
46. Reinstädler, D., Fabian, H., and Naumann, D. (1999) Proteins 34, 303-316
47. Moritz, R., Reinstädler, D., Fabian, H., and Naumann, D. (2002) Biopolymers 67, 145-155
48. Modler, A. J., Gast, K., Lutsch, G., and Damaschun, G. (2003) J. Mol. Biol. 325, 135-148
49. Prusiner, S. B. (1991) Science 252, 1515-1522
50. Serio, T. R., Cashiker, A. G., Kowal, A. S., Sawicki, G. J., Moslehi, J. J., Serpell, L., Arnsdorf, M. F., and Lindquist, S. L. (2000) Science 289, 1317-1321
51. Jarrett, J. T., and Lansbury, P. T., Jr. (1993) Cell 73, 1055-1058
52. Selkoe, D. J. (2002) Science 298, 789-791
53. Volles, M. J., and Lansbury, P. T., Jr. (2002) Biochemistry 41, 4595-4602
54. Vanik, D. L., and Surewicz, W. K. (2002) J. Biol. Chem. 277, 49065-49070
55. Wille, H., Michelitsch, M. D., Guenebaut, V., Supattapone, S., Serban, A., Cohen, F. E., Agard, D. A., and Prusiner, S. B. (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 3563-3568